title: Artificial synthetic receptors as regulators of protein activity.
abstract: This article discusses most recent work and progress in the direction of a rational design of small molecule receptors that efficiently interfere with the biological function of a particular receptor or enzyme-some of which are therapeutically relevant. More specifically, the following topics are highlighted here: the inhibition of voltage-dependent potassium channels of the K(v)1.x family by designed porphyrin and calix[4]arene ligands, the structural and functional recovery of the tetramerization domain of mutated P53 protein by tailored calix[4]arene ligands and the control over LDH activity by supramolecular signaling. Finally a new way to modulate NAD(+)-dependent enzymatic activities by molecular clips and tweezers is presented.
authors.affiliation: Department of Chemistry, University of Duisburg-Essen, Universitätsstr. 7, 45117 Essen, Germany.
authors.forename: Som
authors.initials: S
authors.lastname: Dutt
authors.forename: Constanze
authors.initials: C
authors.lastname: Wilch
authors.forename: Thomas
authors.initials: T
authors.lastname: Schrader
mesh_terms: D015195:Drug Design; D006801:Humans; D008024:Ligands; D011506:Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D054852:Small Molecule Libraries / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*
chemical_list: D008024:Ligands; D011506:Proteins; D054852:Small Molecule Libraries